COX2_BOVIN
ID COX2_BOVIN Reviewed; 227 AA.
AC P68530; P00404;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 138.
DE RecName: Full=Cytochrome c oxidase subunit 2;
DE EC=7.1.1.9;
DE AltName: Full=Cytochrome c oxidase polypeptide II;
GN Name=MT-CO2; Synonyms=COII, COX2, COXII, MTCO2;
OS Bos taurus (Bovine).
OG Mitochondrion.
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Bovinae; Bos.
OX NCBI_TaxID=9913;
RN [1]
RP PROTEIN SEQUENCE, AND FORMYLATION AT MET-1.
RC STRAIN=Hereford {ECO:0000312|Proteomes:UP000009136}; TISSUE=Heart;
RX PubMed=220175;
RA Steffens G.J., Buse G.;
RT "Studies on cytochrome c oxidase, IV[1-3]. Primary structure and function
RT of subunit II.";
RL Hoppe-Seyler's Z. Physiol. Chem. 360:613-619(1979).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Heart;
RX PubMed=7120390; DOI=10.1016/0022-2836(82)90137-1;
RA Anderson S., de Bruijn M.H.L., Coulson A.R., Eperon I.C., Sanger F.,
RA Young I.G.;
RT "Complete sequence of bovine mitochondrial DNA. Conserved features of the
RT mammalian mitochondrial genome.";
RL J. Mol. Biol. 156:683-717(1982).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6265319; DOI=10.1016/0378-1119(80)90108-0;
RA Young I.G., Anderson S.;
RT "The genetic code in bovine mitochondria: sequence of genes for the
RT cytochrome oxidase subunit II and two tRNAs.";
RL Gene 12:257-265(1980).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC STRAIN=65, 66, D, and F;
RA Wettstein P.J.;
RT "Bos taurus mitochondrial protein coding regions.";
RL Submitted (MAR-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP SUBUNIT.
RX PubMed=26698328; DOI=10.1074/jbc.m115.680553;
RA Shinzawa-Itoh K., Shimomura H., Yanagisawa S., Shimada S., Takahashi R.,
RA Oosaki M., Ogura T., Tsukihara T.;
RT "Purification of active respiratory supercomplex from bovine heart
RT mitochondria enables functional studies.";
RL J. Biol. Chem. 291:4178-4184(2016).
RN [6]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RX PubMed=8638158; DOI=10.1126/science.272.5265.1136;
RA Tsukihara T., Aoyama H., Yamashita E., Tomizaki T., Yamaguchi H.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "The whole structure of the 13-subunit oxidized cytochrome c oxidase at 2.8
RT A.";
RL Science 272:1136-1144(1996).
RN [7]
RP X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10089392; DOI=10.1107/s0907444998006362;
RA Tomizaki T., Yamashita E., Yamaguchi H., Aoyama H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yaono R., Yoshikawa S.;
RT "Structure analysis of bovine heart cytochrome c oxidase at 2.8 A
RT resolution.";
RL Acta Crystallogr. D 55:31-45(1999).
RN [8]
RP X-RAY CRYSTALLOGRAPHY (2.9 ANGSTROMS).
RC TISSUE=Heart;
RX PubMed=10771420; DOI=10.1107/s0907444900002213;
RA Fei M.J., Yamashita E., Inoue N., Yao M., Yamaguchi H., Tsukihara T.,
RA Shinzawa-Itoh K., Nakashima R., Yoshikawa S.;
RT "X-ray structure of azide-bound fully oxidized cytochrome c oxidase from
RT bovine heart at 2.9 A resolution.";
RL Acta Crystallogr. D 56:529-535(2000).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (1.80 ANGSTROMS).
RX PubMed=20385840; DOI=10.1073/pnas.0910410107;
RA Muramoto K., Ohta K., Shinzawa-Itoh K., Kanda K., Taniguchi M.,
RA Nabekura H., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "Bovine cytochrome c oxidase structures enable O2 reduction with
RT minimization of reactive oxygens and provide a proton-pumping gate.";
RL Proc. Natl. Acad. Sci. U.S.A. 107:7740-7745(2010).
RN [10]
RP STRUCTURE BY ELECTRON MICROSCOPY (9.10 ANGSTROMS).
RX PubMed=27830641; DOI=10.7554/elife.21290;
RA Sousa J.S., Mills D.J., Vonck J., Kuehlbrandt W.;
RT "Functional asymmetry and electron flow in the bovine respirasome.";
RL Elife 5:0-0(2016).
RN [11]
RP X-RAY CRYSTALLOGRAPHY (1.50 ANGSTROMS).
RX PubMed=27605664; DOI=10.1074/jbc.m115.711770;
RA Yano N., Muramoto K., Shimada A., Takemura S., Baba J., Fujisawa H.,
RA Mochizuki M., Shinzawa-Itoh K., Yamashita E., Tsukihara T., Yoshikawa S.;
RT "The Mg2+-containing water cluster of mammalian cytochrome c oxidase
RT collects four pumping proton equivalents in each catalytic cycle.";
RL J. Biol. Chem. 291:23882-23894(2016).
RN [12]
RP X-RAY CRYSTALLOGRAPHY (1.85 ANGSTROMS).
RX PubMed=31533957; DOI=10.1073/pnas.1907183116;
RA Shinzawa-Itoh K., Sugimura T., Misaki T., Tadehara Y., Yamamoto S.,
RA Hanada M., Yano N., Nakagawa T., Uene S., Yamada T., Aoyama H.,
RA Yamashita E., Tsukihara T., Yoshikawa S., Muramoto K.;
RT "Monomeric structure of an active form of bovine cytochrome c oxidase.";
RL Proc. Natl. Acad. Sci. U.S.A. 116:19945-19951(2019).
CC -!- FUNCTION: Component of the cytochrome c oxidase, the last enzyme in the
CC mitochondrial electron transport chain which drives oxidative
CC phosphorylation. The respiratory chain contains 3 multisubunit
CC complexes succinate dehydrogenase (complex II, CII), ubiquinol-
CC cytochrome c oxidoreductase (cytochrome b-c1 complex, complex III,
CC CIII) and cytochrome c oxidase (complex IV, CIV), that cooperate to
CC transfer electrons derived from NADH and succinate to molecular oxygen,
CC creating an electrochemical gradient over the inner membrane that
CC drives transmembrane transport and the ATP synthase. Cytochrome c
CC oxidase is the component of the respiratory chain that catalyzes the
CC reduction of oxygen to water. Electrons originating from reduced
CC cytochrome c in the intermembrane space (IMS) are transferred via the
CC dinuclear copper A center (CU(A)) of subunit 2 and heme A of subunit 1
CC to the active site in subunit 1, a binuclear center (BNC) formed by
CC heme A3 and copper B (CU(B)). The BNC reduces molecular oxygen to 2
CC water molecules using 4 electrons from cytochrome c in the IMS and 4
CC protons from the mitochondrial matrix. {ECO:0000250|UniProtKB:P00410}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=4 Fe(II)-[cytochrome c] + 8 H(+)(in) + O2 = 4 Fe(III)-
CC [cytochrome c] + 4 H(+)(out) + 2 H2O; Xref=Rhea:RHEA:11436,
CC Rhea:RHEA-COMP:10350, Rhea:RHEA-COMP:14399, ChEBI:CHEBI:15377,
CC ChEBI:CHEBI:15378, ChEBI:CHEBI:15379, ChEBI:CHEBI:29033,
CC ChEBI:CHEBI:29034; EC=7.1.1.9;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC PhysiologicalDirection=left-to-right; Xref=Rhea:RHEA:11437;
CC Evidence={ECO:0000250|UniProtKB:P00410};
CC -!- COFACTOR:
CC Name=Cu cation; Xref=ChEBI:CHEBI:23378;
CC Evidence={ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158};
CC Note=Binds a dinuclear copper A center per subunit.
CC {ECO:0000269|PubMed:20385840, ECO:0000269|PubMed:8638158};
CC -!- SUBUNIT: Component of the cytochrome c oxidase (complex IV, CIV), a
CC multisubunit enzyme composed of 14 subunits. The complex is composed of
CC a catalytic core of 3 subunits MT-CO1, MT-CO2 and MT-CO3, encoded in
CC the mitochondrial DNA, and 11 supernumerary subunits COX4I1 (or
CC COX4I2), COX5A, COX5B, COX6A2 (or COX6A1), COX6B1 (or COX6B2), COX6C,
CC COX7A1 (or COX7A2), COX7B, COX7C, COX8B and NDUFA4, which are encoded
CC in the nuclear genome (PubMed:8638158). The complex exists as a monomer
CC or a dimer and forms supercomplexes (SCs) in the inner mitochondrial
CC membrane with NADH-ubiquinone oxidoreductase (complex I, CI) and
CC ubiquinol-cytochrome c oxidoreductase (cytochrome b-c1 complex, complex
CC III, CIII), resulting in different assemblies (supercomplex
CC SCI(1)III(2)IV(1) and megacomplex MCI(2)III(2)IV(2)) (PubMed:26698328,
CC PubMed:27830641). Found in a complex with TMEM177, COA6, COX18, COX20,
CC SCO1 and SCO2. Interacts with TMEM177 in a COX20-dependent manner.
CC Interacts with COX20. Interacts with COX16 (By similarity).
CC {ECO:0000250|UniProtKB:P00403, ECO:0000269|PubMed:26698328,
CC ECO:0000269|PubMed:27830641, ECO:0000269|PubMed:8638158}.
CC -!- SUBCELLULAR LOCATION: Mitochondrion inner membrane
CC {ECO:0000269|PubMed:27605664, ECO:0000269|PubMed:31533957}; Multi-pass
CC membrane protein {ECO:0000269|PubMed:27605664,
CC ECO:0000269|PubMed:31533957}.
CC -!- SIMILARITY: Belongs to the cytochrome c oxidase subunit 2 family.
CC {ECO:0000305}.
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DR EMBL; V00654; CAA24000.1; -; Genomic_DNA.
DR EMBL; M10544; AAA31644.1; -; Genomic_DNA.
DR EMBL; AF490528; AAM08331.1; -; Genomic_DNA.
DR EMBL; AF490529; AAM08344.1; -; Genomic_DNA.
DR EMBL; AF493541; AAM12792.1; -; Genomic_DNA.
DR EMBL; AF493542; AAM12805.1; -; Genomic_DNA.
DR PIR; B00152; OBBO2.
DR RefSeq; YP_209208.1; NC_006853.1.
DR PDB; 1OCC; X-ray; 2.80 A; B/O=1-227.
DR PDB; 1OCO; X-ray; 2.80 A; B/O=1-227.
DR PDB; 1OCR; X-ray; 2.35 A; B/O=1-227.
DR PDB; 1OCZ; X-ray; 2.90 A; B/O=1-227.
DR PDB; 1V54; X-ray; 1.80 A; B/O=1-227.
DR PDB; 1V55; X-ray; 1.90 A; B/O=1-227.
DR PDB; 2DYR; X-ray; 1.80 A; B/O=1-227.
DR PDB; 2DYS; X-ray; 2.20 A; B/O=1-227.
DR PDB; 2EIJ; X-ray; 1.90 A; B/O=1-227.
DR PDB; 2EIK; X-ray; 2.10 A; B/O=1-227.
DR PDB; 2EIL; X-ray; 2.10 A; B/O=1-227.
DR PDB; 2EIM; X-ray; 2.60 A; B/O=1-227.
DR PDB; 2EIN; X-ray; 2.70 A; B/O=1-227.
DR PDB; 2OCC; X-ray; 2.30 A; B/O=1-227.
DR PDB; 2Y69; X-ray; 1.95 A; B/O=1-227.
DR PDB; 2YBB; EM; 19.00 A; M=1-227.
DR PDB; 2ZXW; X-ray; 2.50 A; B/O=1-227.
DR PDB; 3ABK; X-ray; 2.00 A; B/O=1-227.
DR PDB; 3ABL; X-ray; 2.10 A; B/O=1-227.
DR PDB; 3ABM; X-ray; 1.95 A; B/O=1-227.
DR PDB; 3AG1; X-ray; 2.20 A; B/O=1-227.
DR PDB; 3AG2; X-ray; 1.80 A; B/O=1-227.
DR PDB; 3AG3; X-ray; 1.80 A; B/O=1-227.
DR PDB; 3AG4; X-ray; 2.05 A; B/O=1-227.
DR PDB; 3ASN; X-ray; 3.00 A; B/O=1-227.
DR PDB; 3ASO; X-ray; 2.30 A; B/O=1-227.
DR PDB; 3WG7; X-ray; 1.90 A; B/O=1-227.
DR PDB; 3X2Q; X-ray; 2.00 A; B/O=1-227.
DR PDB; 5B1A; X-ray; 1.50 A; B/O=1-227.
DR PDB; 5B1B; X-ray; 1.60 A; B/O=1-227.
DR PDB; 5B3S; X-ray; 1.68 A; B/O=2-227.
DR PDB; 5GPN; EM; 5.40 A; z=1-227.
DR PDB; 5IY5; X-ray; 2.00 A; B/O=1-227.
DR PDB; 5LUF; EM; 9.10 A; y=1-227.
DR PDB; 5W97; X-ray; 2.30 A; B/b=1-227.
DR PDB; 5WAU; X-ray; 1.95 A; B/b=1-227.
DR PDB; 5X19; X-ray; 2.20 A; B/O=1-227.
DR PDB; 5X1B; X-ray; 2.40 A; B/O=1-227.
DR PDB; 5X1F; X-ray; 2.20 A; B/O=1-227.
DR PDB; 5XDQ; X-ray; 1.77 A; B/O=1-227.
DR PDB; 5XDX; X-ray; 1.99 A; B/O=1-227.
DR PDB; 5XTH; EM; 3.90 A; y=1-227.
DR PDB; 5XTI; EM; 17.40 A; By/y=1-227.
DR PDB; 5Z84; X-ray; 1.85 A; B/O=1-227.
DR PDB; 5Z85; X-ray; 1.85 A; B/O=1-227.
DR PDB; 5Z86; X-ray; 1.85 A; B/O=1-227.
DR PDB; 5ZCO; X-ray; 1.90 A; B/O=1-227.
DR PDB; 5ZCP; X-ray; 1.65 A; B/O=1-227.
DR PDB; 5ZCQ; X-ray; 1.65 A; B/O=1-227.
DR PDB; 6J8M; X-ray; 1.90 A; B/O=1-227.
DR PDB; 6JUW; X-ray; 1.80 A; B/O=1-227.
DR PDB; 6JY3; X-ray; 1.85 A; B=1-227.
DR PDB; 6JY4; X-ray; 1.95 A; B=1-227.
DR PDB; 6NKN; X-ray; 2.50 A; B/O=1-227.
DR PDB; 6NMF; X-ray; 2.80 A; B/O=1-227.
DR PDB; 6NMP; X-ray; 2.90 A; B/O=1-227.
DR PDB; 7COH; X-ray; 1.30 A; B/O=1-227.
DR PDB; 7CP5; X-ray; 1.76 A; B/O=1-227.
DR PDB; 7D5W; X-ray; 1.84 A; B/O=1-227.
DR PDB; 7D5X; X-ray; 1.74 A; B/O=1-227.
DR PDB; 7EV7; X-ray; 1.70 A; B/O=1-227.
DR PDB; 7THU; X-ray; 1.93 A; BBB/OOO=1-227.
DR PDB; 7TIE; X-ray; 1.90 A; BBB/OOO=1-227.
DR PDB; 7TIH; X-ray; 2.35 A; BBB/OOO=1-227.
DR PDB; 7TII; X-ray; 2.45 A; BBB/OOO=1-227.
DR PDBsum; 1OCC; -.
DR PDBsum; 1OCO; -.
DR PDBsum; 1OCR; -.
DR PDBsum; 1OCZ; -.
DR PDBsum; 1V54; -.
DR PDBsum; 1V55; -.
DR PDBsum; 2DYR; -.
DR PDBsum; 2DYS; -.
DR PDBsum; 2EIJ; -.
DR PDBsum; 2EIK; -.
DR PDBsum; 2EIL; -.
DR PDBsum; 2EIM; -.
DR PDBsum; 2EIN; -.
DR PDBsum; 2OCC; -.
DR PDBsum; 2Y69; -.
DR PDBsum; 2YBB; -.
DR PDBsum; 2ZXW; -.
DR PDBsum; 3ABK; -.
DR PDBsum; 3ABL; -.
DR PDBsum; 3ABM; -.
DR PDBsum; 3AG1; -.
DR PDBsum; 3AG2; -.
DR PDBsum; 3AG3; -.
DR PDBsum; 3AG4; -.
DR PDBsum; 3ASN; -.
DR PDBsum; 3ASO; -.
DR PDBsum; 3WG7; -.
DR PDBsum; 3X2Q; -.
DR PDBsum; 5B1A; -.
DR PDBsum; 5B1B; -.
DR PDBsum; 5B3S; -.
DR PDBsum; 5GPN; -.
DR PDBsum; 5IY5; -.
DR PDBsum; 5LUF; -.
DR PDBsum; 5W97; -.
DR PDBsum; 5WAU; -.
DR PDBsum; 5X19; -.
DR PDBsum; 5X1B; -.
DR PDBsum; 5X1F; -.
DR PDBsum; 5XDQ; -.
DR PDBsum; 5XDX; -.
DR PDBsum; 5XTH; -.
DR PDBsum; 5XTI; -.
DR PDBsum; 5Z84; -.
DR PDBsum; 5Z85; -.
DR PDBsum; 5Z86; -.
DR PDBsum; 5ZCO; -.
DR PDBsum; 5ZCP; -.
DR PDBsum; 5ZCQ; -.
DR PDBsum; 6J8M; -.
DR PDBsum; 6JUW; -.
DR PDBsum; 6JY3; -.
DR PDBsum; 6JY4; -.
DR PDBsum; 6NKN; -.
DR PDBsum; 6NMF; -.
DR PDBsum; 6NMP; -.
DR PDBsum; 7COH; -.
DR PDBsum; 7CP5; -.
DR PDBsum; 7D5W; -.
DR PDBsum; 7D5X; -.
DR PDBsum; 7EV7; -.
DR PDBsum; 7THU; -.
DR PDBsum; 7TIE; -.
DR PDBsum; 7TIH; -.
DR PDBsum; 7TII; -.
DR AlphaFoldDB; P68530; -.
DR SMR; P68530; -.
DR CORUM; P68530; -.
DR DIP; DIP-39024N; -.
DR IntAct; P68530; 2.
DR STRING; 9913.ENSBTAP00000053151; -.
DR TCDB; 3.D.4.7.1; the proton-translocating cytochrome oxidase (cox) superfamily.
DR iPTMnet; P68530; -.
DR PaxDb; P68530; -.
DR PeptideAtlas; P68530; -.
DR PRIDE; P68530; -.
DR Ensembl; ENSBTAT00000060549; ENSBTAP00000053151; ENSBTAG00000043556.
DR GeneID; 3283880; -.
DR KEGG; bta:3283880; -.
DR CTD; 4513; -.
DR VEuPathDB; HostDB:ENSBTAG00000043556; -.
DR eggNOG; KOG4767; Eukaryota.
DR GeneTree; ENSGT00390000017410; -.
DR HOGENOM; CLU_036876_2_3_1; -.
DR InParanoid; P68530; -.
DR OMA; WSYEYTD; -.
DR OrthoDB; 1432833at2759; -.
DR TreeFam; TF344269; -.
DR Reactome; R-BTA-5628897; TP53 Regulates Metabolic Genes.
DR Reactome; R-BTA-611105; Respiratory electron transport.
DR Reactome; R-BTA-9707564; Cytoprotection by HMOX1.
DR EvolutionaryTrace; P68530; -.
DR Proteomes; UP000009136; Mitochondrion.
DR Bgee; ENSBTAG00000043556; Expressed in tongue muscle and 104 other tissues.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005751; C:mitochondrial respiratory chain complex IV; IEA:Ensembl.
DR GO; GO:0045277; C:respiratory chain complex IV; IDA:UniProtKB.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0004129; F:cytochrome-c oxidase activity; IEA:UniProtKB-EC.
DR CDD; cd13912; CcO_II_C; 1.
DR Gene3D; 1.10.287.90; -; 1.
DR Gene3D; 2.60.40.420; -; 1.
DR InterPro; IPR045187; CcO_II.
DR InterPro; IPR002429; CcO_II-like_C.
DR InterPro; IPR034210; CcO_II_C.
DR InterPro; IPR001505; Copper_CuA.
DR InterPro; IPR008972; Cupredoxin.
DR InterPro; IPR014222; Cyt_c_oxidase_su2.
DR InterPro; IPR011759; Cyt_c_oxidase_su2_TM_dom.
DR InterPro; IPR036257; Cyt_c_oxidase_su2_TM_sf.
DR PANTHER; PTHR22888; PTHR22888; 1.
DR Pfam; PF00116; COX2; 1.
DR Pfam; PF02790; COX2_TM; 1.
DR SUPFAM; SSF49503; SSF49503; 1.
DR SUPFAM; SSF81464; SSF81464; 1.
DR TIGRFAMs; TIGR02866; CoxB; 1.
DR PROSITE; PS00078; COX2; 1.
DR PROSITE; PS50857; COX2_CUA; 1.
DR PROSITE; PS50999; COX2_TM; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Copper; Direct protein sequencing; Electron transport;
KW Formylation; Magnesium; Membrane; Metal-binding; Mitochondrion;
KW Mitochondrion inner membrane; Phosphoprotein; Reference proteome;
KW Respiratory chain; Translocase; Transmembrane; Transmembrane helix;
KW Transport.
FT CHAIN 1..227
FT /note="Cytochrome c oxidase subunit 2"
FT /id="PRO_0000183517"
FT TOPO_DOM 1..14
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 15..45
FT /note="Helical; Name=I"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 46..59
FT /note="Mitochondrial matrix"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TRANSMEM 60..87
FT /note="Helical; Name=II"
FT /evidence="ECO:0000269|PubMed:27605664"
FT TOPO_DOM 88..227
FT /note="Mitochondrial intermembrane"
FT /evidence="ECO:0000269|PubMed:27605664"
FT BINDING 161
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 196
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 198
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 198
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /ligand_note="ligand shared with MT-CO1"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 200
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 204
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A2"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT BINDING 207
FT /ligand="Cu cation"
FT /ligand_id="ChEBI:CHEBI:23378"
FT /ligand_label="A1"
FT /evidence="ECO:0000269|PubMed:20385840,
FT ECO:0000269|PubMed:8638158"
FT MOD_RES 1
FT /note="N-formylmethionine"
FT /evidence="ECO:0000269|PubMed:220175"
FT MOD_RES 218
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:P00406"
FT CONFLICT 58
FT /note="A -> P (in Ref. 3; AAA31644)"
FT /evidence="ECO:0000305"
FT CONFLICT 118
FT /note="F -> L (in Ref. 3; AAA31644)"
FT /evidence="ECO:0000305"
FT HELIX 15..45
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 59..88
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 94..102
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 105..110
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 116..120
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 125..127
FT /evidence="ECO:0007829|PDB:7COH"
FT TURN 134..136
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 138..140
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 150..159
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 161..165
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 166..168
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 170..174
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 180..184
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 190..194
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 204..206
FT /evidence="ECO:0007829|PDB:7COH"
FT STRAND 209..214
FT /evidence="ECO:0007829|PDB:7COH"
FT HELIX 216..225
FT /evidence="ECO:0007829|PDB:7COH"
SQ SEQUENCE 227 AA; 26021 MW; C562D5B39FA9771A CRC64;
MAYPMQLGFQ DATSPIMEEL LHFHDHTLMI VFLISSLVLY IISLMLTTKL THTSTMDAQE
VETIWTILPA IILILIALPS LRILYMMDEI NNPSLTVKTM GHQWYWSYEY TDYEDLSFDS
YMIPTSELKP GELRLLEVDN RVVLPMEMTI RMLVSSEDVL HSWAVPSLGL KTDAIPGRLN
QTTLMSSRPG LYYGQCSEIC GSNHSFMPIV LELVPLKYFE KWSASML
